Gene structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its gene transcription under different light intensities

Koki Mukai, Ayano Teramoto, Xuchun Qiu, Yohei Shimasaki, Yoko Kato-Unoki, Man Lee, Naohiro Mizoguchi, Mst Ruhina Margia Khanam, Hina Satone, Tsuneyuki Tatsuke, Takahiro Kusakabe, Yuji Oshima

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Abstract

We investigated the gene structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx gene relative to several others (ycf59–2-CysPrx–rpl35–rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcript levels of 2-Cys Prx in C. marina cells grown under three different light intensities (0, 100, 1000 µmol photons m–2 s–1, 14-h light/8-h dark photoperiod) by quantitative PCR. The 2-Cys Prx transcript level in cells grown under the highest light intensity on day 3 was threefold that on day 0 but two lower light intensities resulted in relatively stable transcription levels. The 2-Cys Prx transcript level was significantly positively related to the H2O2 concentration per cell and the H2O2 scavenging activity per cell. These results suggest that C. marina 2-Cys Prx functions in the chloroplast and its transcription could be regulated by both NEP and PEP. Moreover, the 2-Cys Prx transcript level might increase to remove excessive H2O2 produced under strong light conditions in order to maintain cell proliferation activity.

Original languageEnglish
Pages (from-to)29-38
Number of pages10
JournalEuropean Journal of Phycology
Volume53
Issue number1
DOIs
Publication statusPublished - Jan 2 2018

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peroxiredoxin
marina
algal blooms
light intensity
plastid
algal bloom
transcription (genetics)
amino acid
gene
chloroplast
RNA
genes
plastids
photoperiod
antioxidant
DNA-directed RNA polymerase
genome
enzyme
amino acid sequences
protein

All Science Journal Classification (ASJC) codes

  • Aquatic Science
  • Plant Science

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Gene structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its gene transcription under different light intensities. / Mukai, Koki; Teramoto, Ayano; Qiu, Xuchun; Shimasaki, Yohei; Kato-Unoki, Yoko; Lee, Man; Mizoguchi, Naohiro; Margia Khanam, Mst Ruhina; Satone, Hina; Tatsuke, Tsuneyuki; Kusakabe, Takahiro; Oshima, Yuji.

In: European Journal of Phycology, Vol. 53, No. 1, 02.01.2018, p. 29-38.

Research output: Contribution to journalArticle

Mukai, Koki ; Teramoto, Ayano ; Qiu, Xuchun ; Shimasaki, Yohei ; Kato-Unoki, Yoko ; Lee, Man ; Mizoguchi, Naohiro ; Margia Khanam, Mst Ruhina ; Satone, Hina ; Tatsuke, Tsuneyuki ; Kusakabe, Takahiro ; Oshima, Yuji. / Gene structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its gene transcription under different light intensities. In: European Journal of Phycology. 2018 ; Vol. 53, No. 1. pp. 29-38.
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abstract = "We investigated the gene structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx gene relative to several others (ycf59–2-CysPrx–rpl35–rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcript levels of 2-Cys Prx in C. marina cells grown under three different light intensities (0, 100, 1000 µmol photons m–2 s–1, 14-h light/8-h dark photoperiod) by quantitative PCR. The 2-Cys Prx transcript level in cells grown under the highest light intensity on day 3 was threefold that on day 0 but two lower light intensities resulted in relatively stable transcription levels. The 2-Cys Prx transcript level was significantly positively related to the H2O2 concentration per cell and the H2O2 scavenging activity per cell. These results suggest that C. marina 2-Cys Prx functions in the chloroplast and its transcription could be regulated by both NEP and PEP. Moreover, the 2-Cys Prx transcript level might increase to remove excessive H2O2 produced under strong light conditions in order to maintain cell proliferation activity.",
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AU - Kato-Unoki, Yoko

AU - Lee, Man

AU - Mizoguchi, Naohiro

AU - Margia Khanam, Mst Ruhina

AU - Satone, Hina

AU - Tatsuke, Tsuneyuki

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